5k95: Difference between revisions

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 ==Crystal Structure of GTP Cyclohydrolase-IB with 8-oxo-GTP==
-<StructureSection load='5k95' size='340' side='right' caption='[[5k95]], [[Resolution|resolution]] 2.77&Aring;' scene=''>
+<StructureSection load='5k95' size='340' side='right'caption='[[5k95]], [[Resolution|resolution]] 2.77&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5k95]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K95 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K95 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5k95]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Neig1 Neig1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K95 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K95 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8GT:8-OXO-GUANOSINE-5-TRIPHOSPHATE'>8GT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SNC:S-NITROSO-CYSTEINE'>SNC</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5k9g|5k9g]]</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">folE2, NGO0387 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=242231 NEIG1])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/GTP_cyclohydrolase_I GTP cyclohydrolase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.16 3.5.4.16] </span></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5k95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k95 OCA], [http://pdbe.org/5k95 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k95 RCSB], [http://www.ebi.ac.uk/pdbsum/5k95 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k95 ProSAT]</span></td></tr>
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 == Function ==
 [[http://www.uniprot.org/uniprot/GCH4_NEIG1 GCH4_NEIG1]] Converts GTP to 7,8-dihydroneopterin triphosphate.<ref>PMID:17032654</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Guanosine 5'-triphosphate (GTP) cyclohydrolase-I (GCYH-I) catalyzes the first step in folic acid biosynthesis in bacteria and plants, biopterin biosynthesis in mammals, and the biosynthesis of 7-deazaguanosine-modified tRNA nucleosides in bacteria and archaea. The type IB GCYH (GCYH-IB) is a prokaryotic-specific enzyme found in many pathogens. GCYH-IB is structurally distinct from the canonical type IA GCYH involved in biopterin biosynthesis in humans and animals, and thus is of interest as a potential antibacterial drug target. We report kinetic and inhibition data of Neisseria gonorrhoeae GCYH-IB and two high-resolution crystal structures of the enzyme; one in complex with the reaction intermediate analog and competitive inhibitor 8-oxoguanosine 5'-triphosphate (8-oxo-GTP), and one with a tris(hydroxymethyl)aminomethane molecule bound in the active site and mimicking another reaction intermediate. Comparison with the type IA enzyme bound to 8-oxo-GTP (guanosine 5'-triphosphate) reveals an inverted mode of binding of the inhibitor ribosyl moiety and, together with site-directed mutagenesis data, shows that the two enzymes utilize different strategies for catalysis. Notably, the inhibitor interacts with a conserved active-site Cys149, and this residue is S-nitrosylated in the structures. This is the first structural characterization of a biologically S-nitrosylated bacterial protein. Mutagenesis and biochemical analyses demonstrate that Cys149 is essential for the cyclohydrolase reaction, and S-nitrosylation maintains enzyme activity, suggesting a potential role of the S-nitrosothiol in catalysis.
+Mechanism and catalytic strategy of the prokaryotic-specific GTP cyclohydrolase-IB.,Paranagama N, Bonnett SA, Alvarez J, Luthra A, Stec B, Gustafson A, Iwata-Reuyl D, Swairjo MA Biochem J. 2017 Mar 7;474(6):1017-1039. doi: 10.1042/BCJ20161025. PMID:28126741<ref>PMID:28126741</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5k95" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cyclohydrolase 3D structures|Cyclohydrolase 3D structures]]
 == References ==
 <references/>
@@ Line 17: / Line 30: @@
 </StructureSection>
 [[Category: GTP cyclohydrolase I]]
+[[Category: Large Structures]]
+[[Category: Neig1]]
 [[Category: Alvarez, J]]
 [[Category: Stec, B]]